GHMP kinase family

In molecular biology, the GHMP kinase family is a family of kinase enzymes. Members of this family include homoserine kinases EC 2.7.1.39, galactokinases EC 2.7.1.6, and mevalonate kinases EC 2.7.1.36. These kinases make up the GHMP kinase superfamily of ATP-dependent enzymes.^[1] These enzymes are involved in the biosynthesis of isoprenes and amino acids as well as in carbohydrate metabolism. These enzymes contain, in their N-terminal section, a conserved Gly/Ser-rich region which is probably involved in the binding of ATP.^[2]^[3] The C-terminal domain of homoserine kinase has a central alpha-beta plait fold and an insertion of four helices, which, together with the N-terminal fold, creates a novel nucleotide binding fold.^[4]

References

^ Bork P, Sander C, Valencia A (January 1993). "Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases". Protein Sci. 2 (1): 31–40. doi:10.1002/pro.5560020104. PMC 2142297. PMID 8382990.
^ Tsay YH, Robinson GW (February 1991). "Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase". Mol. Cell. Biol. 11 (2): 620–31. doi:10.1128/MCB.11.2.620. PMC 359713. PMID 1846667.
^ Lee M, Leustek T (December 1999). "Identification of the gene encoding homoserine kinase from Arabidopsis thaliana and characterization of the recombinant enzyme derived from the gene". Arch. Biochem. Biophys. 372 (1): 135–42. doi:10.1006/abbi.1999.1481. PMID 10562426.
^ Zhou T, Daugherty M, Grishin NV, Osterman AL, Zhang H (December 2000). "Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily". Structure. 8 (12): 1247–57. doi:10.1016/s0969-2126(00)00533-5. PMID 11188689.

This article incorporates text from the public domain Pfam and InterPro: IPR013750

This article incorporates text from the public domain Pfam and InterPro: IPR006204

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